Purification and partial sequence of the rabbit mammary gland prolactin receptor.
1. The prolactin receptor from rabbit mammary gland was purified to near homogeneity using a novel hydrophobic interaction chromatographic procedure. 2. Part sequencing (101 residues) revealed 34% identity with the rabbit liver growth hormone receptor, providing support for the existence of a new class of transmembrane receptors regulating growth and lactation.
Waters
M J
MJ
Department of Physiology and Pharmacology, University of Queensland, St. Lucia, Australia.
Spencer
S A
SA
Hamlin
G
G
Henzel
W J
WJ
Wood
W I
WI
D000595:Amino Acid Sequence; D000818:Animals; D002845:Chromatography; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases; D005260:Female; D007425:Intracellular Membranes / Q000737:chemistry; D008099:Liver / Q000737:chemistry; D008321:Mammary Glands, Animal / Q000737:chemistry* / Q000648:ultrastructure; D008861:Microsomes / Q000737:chemistry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D011817:Rabbits; D011981:Receptors, Prolactin / Q000737:chemistry / Q000302:isolation & purification*; D011986:Receptors, Somatotropin / Q000737:chemistry; D012689:Sequence Homology, Nucleic Acid
D010446:Peptide Fragments; D011981:Receptors, Prolactin; D011986:Receptors, Somatotropin; D010450:Endopeptidases; C044574:lysine-C peptidase